EC Number   |
General Information |
Reference |
|---|
   1.14.11.6 | more |
molecular basis for substrate specificity and catalytic mechanism of the enzyme and molecular mechanism of substrate recognition, overview. Residues Phe292, Tyr217 and Arg190 play critical roles in substrate binding and catalysis, and the interactions of the C5 modification group of substrates with the cosubstrate and enzyme contribute to the slightly varied binding affinity and activity towards different substrates. After the catalysis, the products are released and new cosubstrate and substrate are reloaded to conduct the next oxidation reaction. Active site structure, and 2-oxoglutarate binding structure, binding affinity of the enzyme for different substrates, overview. Residue Arg286 plays an important role in the binding of 2-oxoglutarate, Arg190 plays a vital role in the binding of both 2-oxoglutarate and the substrate, and Phe292 and Tyr217 play critical roles in the substrate binding |
745921 |
| 1.14.11.6 | physiological function |
telomeric DNA of Trypanosomatids possesses a modified thymine base, called base J or beta-D-glucopyranosyloxymethyluracil, that is synthesized in a two-step process. The base is hydroxylated by a thymidine hydroxylase forming hydroxymethyluracil (hmU), a glucose moiety is then attached by the J-associated glucosyltransferase (JGT). Both JBP1 and JBP2 stimulate de novo thymidine hydroxylation in vivo. DNA Jaylation is largely regulated by cis-acting sequences and is thus genetically encoded. The key regulatory step of J synthesis seems to be the first step catalyzed by JBP1 and JBP2. The specificity of base J localization is probably due to the JBP enzymes generating 5-hydroxymethyluracil at only specific sites throughout the genome |
745735 |
| 1.14.11.6 | physiological function |
the genomic DNA of kinetoplastid parasites contains a unique modified base beta-D-glucosylhydroxymethyluracil or base J. J-binding protein, JBP, 1 and 2, which regulate the levels of J in the genome, are catalyzing the first step in J biosynthesis. JBP2, like JBP1, is a thymidine hydroxylase. Unlike JBP1, JBP2 is dispensable for Leishmania, mutational analysis, overview |
700084 |
